1999
DOI: 10.1016/s0014-5793(99)00793-0
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Mutagenesis and crystallographic studies of Zymomonas mobilis tRNA‐guanine transglycosylase to elucidate the role of serine 103 for enzymatic activity

Abstract: The tRNA modifying enzyme tRNA-guanine transglycosylase (TGT) is involved in the exchange of guanine in the first position of the anticodon with preQ 1 as part of the biosynthesis of the hypermodified base queuine (Q). Mutation of Ser 90 to an alanine in Escherichia coli TGT leads to a dramatic reduction of enzymatic activity (Reuter, K. et al. (1994) Biochemistry 33, 7041^7046). To further clarify the role of this residue in the catalytic center, we have mutated the corresponding Ser 103 of the crystallizable… Show more

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Cited by 11 publications
(7 citation statements)
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“…5) to a position more similar to that seen in the Z. mobilis crystal structure. Others have proposed that S90 is used to orient the substrate (11,51), but the distance observed between the ligand and S90 in the simulations and the crystal structure is too long for a proper hydrogen bond. In the farther position seen in the MD of the mutants, S90 is able to coordinate bridging water molecules to complex guanine as noted above.…”
Section: Structural Analysis Of Wt and Mutant Tgtsmentioning
confidence: 99%
See 1 more Smart Citation
“…5) to a position more similar to that seen in the Z. mobilis crystal structure. Others have proposed that S90 is used to orient the substrate (11,51), but the distance observed between the ligand and S90 in the simulations and the crystal structure is too long for a proper hydrogen bond. In the farther position seen in the MD of the mutants, S90 is able to coordinate bridging water molecules to complex guanine as noted above.…”
Section: Structural Analysis Of Wt and Mutant Tgtsmentioning
confidence: 99%
“…Thus, TGT has become a novel target for antishigellosis therapy and possibly broad-spectrum antibiotics. The rational design of TGT inhibitors is an ongoing effort (8)(9)(10)(11), and understanding the molecular recognition of substrates and inhibitors is important to these efforts.…”
Section: Introductionmentioning
confidence: 99%
“…However, the highly homologous (55% sequence identity) TGT from Z. mobilis has been amenable to crystallization and x-ray structure determination (13). Therefore, we have generated the mutation (D280E) in the Z. mobilis TGT that corresponds to D264E in the E. coli TGT following the method of Grä dler et al (22). Z. mobilis TGT(D280E) was purified and crystallized as described previously (13).…”
Section: E Coli Trna-guanine Transglycosylasementioning
confidence: 99%
“…For sterical reasons, this dimer is, although endowed with two active sites, able to bind and convert only one substrate tRNA molecule at a time [17]. The reaction catalysed by bacterial Tgt is accurately documented by numerous biochemical studies and crystal structures of Tgt from Zymomonas mobilis determined in its apo-form, in the presence of guanine, preQ 1 or small molecule inhibitors and in complex with an RNA substrate [16], [18][24]. The reaction follows a ping-pong mechanism including a covalent Tgt⋅tRNA intermediate (Figure 3).…”
Section: Introductionmentioning
confidence: 99%